Use your antibodies-online credentials, if available.
No Products on your Comparison List.
Your basket is empty.
Find out more
Voltage-gated potassium (Kv) channels represent the most complex class of voltage-gated ion channels from both functional and structural standpoints. Additionally we are shipping Potassium Voltage-Gated Channel, Subfamily H (Eag-Related), Member 1 Antibodies (44) and many more products for this protein.
Showing 3 out of 7 products:
Data show that the interaction of beta1 integrins with hERG1 (show KCNH2 Proteins) channels in cancer cells stimulated distinct signaling pathways that depended on the conformational state of hERG1 (show KCNH2 Proteins) and affected different aspects of tumor progression.
Crystal structure of the PAS (show PASK Proteins) domain of the hEAG potassium channel (show KCNAB2 Proteins) has been presented.
KV10.1 localizes to the centrosome and the primary cilium and promotes ciliary disassembly. Interference with KV10.1 ciliary localization abolishes not only the effects on ciliary disassembly, but also KV10.1-induced tumor progression in vivo Conversely.
Mibefradil binds to the voltage sensor domain of Kv10.1 channels, modifying the gating of the channels in a way that in some, but not all, aspects opposes the gating effects exerted by divalent cations.
Eag1 potassium channels and miR34a are involved in the response to rotenone-induced injury in SHSY5Y cells.
The human EAG1 (hEAG1) channel is remarkably sensitive to inhibition by intracellular calcium (Ca(2 (show CA2 Proteins)+) i) through binding of Ca(2 (show CA2 Proteins)+)-calmodulin to three sites adjacent to the eagD and cNBHD.
Structural, biochemical, and functional analysis of the calmodulin (CaM) binding sites within the EAG1 channel suggests that the molecular change induced by CaM and underlying channel inhibition occurs locally.
Our report confirms that KCNH1 mutations are associated with syndromic neurodevelopmental disorder, and also support the functional importance of the S4 domain.
Epilepsy is a key phenotypic feature in most individuals with KCNH1-related syndromes, suggesting a direct role of KCNH1 in epileptogenesis, although the underlying mechanism is not understood.
Findings show that the hEAG1 channel is directly regulated by PIP2 and that this regulation may contribute to normal human physiology and pathology.
KV10.1 (show KCNG3 Proteins) localizes to the centrosome and the primary cilium and promotes ciliary disassembly. Interference with KV10.1 (show KCNG3 Proteins) ciliary localization abolishes not only the effects on ciliary disassembly, but also KV10.1 (show KCNG3 Proteins)-induced tumor progression in vivo Conversely.
Expression of Kv10.1 (show KCNG3 Proteins) driven by phosphorylated Rb/E2F1 (show E2F1 Proteins) contributes to G2/M progression of cancer and non-transformed cells.
deletion of Kv10.1 (show KCNG3 Proteins) does not show a marked phenotype is a prerequisite for utilizing Kv10.1 (show KCNG3 Proteins) blocking and/or reduction techniques, such as siRNA, to treat cancer.
The flavonoids identified here potentiated EAG1 channels by binding to the CNBHD.
2 A resolution crystal structure of the eag domain-CNBHD complex of the mouse EAG1 (also known as KCNH1) channel
X-ray diffraction of EAG channel data were collected to 2.2 A resolution and the crystal belonged to the hexagonal space group P3(1)21
Single crystal of EAG PAS (show PASK Proteins) from Mus (show TRPV6 Proteins) musculus belonging to space group P3221
Ether-a-go-go-related (show KCNH2 Proteins) gene K channels in interstitial cells of Cajal contribute to membrane potential and play role in regulation of pacemaker activity of small intestine.
Eag1 interferes with the cellular mechanism for maintaining oxygen homeostasis, increasing HIF-1 activity, and thereby VEGF secretion and tumor vascularization
Results indicate that cyclic nucleotides do not directly modulate mEAG1 and hERG1 (show KCNH2 Proteins) channels.
These results reveal an unanticipated basic activity of kcnh1 that is crucial for early embryonic development and patterning.
Voltage-gated potassium (Kv) channels represent the most complex class of voltage-gated ion channels from both functional and structural standpoints. Their diverse functions include regulating neurotransmitter release, heart rate, insulin secretion, neuronal excitability, epithelial electrolyte transport, smooth muscle contraction, and cell volume. This gene encodes a member of the potassium channel, voltage-gated, subfamily H. This member is a pore-forming (alpha) subunit of a voltage-gated non-inactivating delayed rectifier potassium channel. It is activated at the onset of myoblast differentiation. The gene is highly expressed in brain and in myoblasts. Overexpression of the gene may confer a growth advantage to cancer cells and favor tumor cell proliferation. Alternative splicing of this gene results in two transcript variants encoding distinct isoforms.
potassium voltage-gated channel, subfamily H (eag-related), member 1
, potassium voltage-gated channel, subfamily H, member 1
, potassium voltage-gated channel, subfamily H, member 1-like
, potassium voltage-gated channel subfamily H member 1-like
, ether-a-go-go potassium channel 1
, potassium voltage-gated channel subfamily H member 1
, voltage-gated potassium channel subunit Kv10.1
, EAG channel 1
, ether-a-go-go, Drosophila, homolog of
, ether a go-go
, potassium voltage-gated channel subfamily H member 1a